scholarly journals Laser-Triggered Small Interfering RNA Releasing Gold Nanoshells against Heat Shock Protein for Sensitized Photothermal Therapy

2016 ◽  
Vol 4 (2) ◽  
pp. 1600327 ◽  
Author(s):  
Zhaohui Wang ◽  
Siwen Li ◽  
Min Zhang ◽  
Yi Ma ◽  
Yuxi Liu ◽  
...  
Keyword(s):  
Heat Shock ◽  
Heat Shock Protein ◽  
Photothermal Therapy ◽  
Small Interfering Rna ◽  
Gold Nanoshells ◽  
Interfering Rna

scholarly journals Synthetic small interfering RNA targeting heat shock protein 105 induces apoptosis of various cancer cells both in vitro and in vivo

2006 ◽  
Vol 97 (7) ◽  
pp. 623-632 ◽  
Author(s):  
Seiji Hosaka ◽  
Tetsuya Nakatsura ◽  
Hirotake Tsukamoto ◽  
Takumi Hatayama ◽  
Hideo Baba ◽  
...  
Keyword(s):  
Heat Shock ◽  
Heat Shock Protein ◽  
Cancer Cells ◽  
Small Interfering Rna ◽  
Rna Targeting ◽  
Interfering Rna

scholarly journals Pseudogenes

2012 ◽  
Vol 2012 ◽  
pp. 1-4 ◽  
Author(s):  
Yusuf Tutar
Keyword(s):  
Gene Regulation ◽  
Heat Shock ◽  
Heat Shock Protein ◽  
Tumor Suppressors ◽  
Small Interfering Rna ◽  
Current Knowledge ◽  
Heat Shock Protein 90 ◽  
A Genome ◽  
Interfering Rna ◽  
Mirna Concentration

Pseudogenes are ubiquitous and abundant in genomes. Pseudogenes were once called “genomic fossils” and treated as “junk DNA” several years. Nevertheless, it has been recognized that some pseudogenes play essential roles in gene regulation of their parent genes, and many pseudogenes are transcribed into RNA. Pseudogene transcripts may also form small interfering RNA or decrease cellular miRNA concentration. Thus, pseudogenes regulate tumor suppressors and oncogenes. Their essential functions draw the attention of our research group in my current work on heat shock protein 90: a chaperone of oncogenes. The paper reviews our current knowledge on pseudogenes and evaluates preliminary results of the chaperone data. Current efforts to understand pseudogenes interactions help to understand the functions of a genome.

Selectively Sensitizing Malignant Cells to Photothermal Therapy Using a CD44-Targeting Heat Shock Protein 72 Depletion Nanosystem

ACS Nano ◽  
2016 ◽  
Vol 10 (9) ◽  
pp. 8578-8590 ◽  
Author(s):  
Shouju Wang ◽  
Ying Tian ◽  
Wei Tian ◽  
Jing Sun ◽  
Shuang Zhao ◽  
...  
Keyword(s):  
Heat Shock ◽  
Heat Shock Protein ◽  
Photothermal Therapy ◽  
Malignant Cells ◽  
Heat Shock Protein 72 ◽  
Cd44 Targeting

scholarly journals Anaphase-Promoting Complex/Cyclosome Participates in the Acute Response to Protein-Damaging Stress

2010 ◽  
Vol 30 (24) ◽  
pp. 5608-5620 ◽  
Author(s):  
Johanna K. Ahlskog ◽  
Johanna K. Björk ◽  
Alexandra N. Elsing ◽  
Camilla Aspelin ◽  
Marko Kallio ◽  
...  
Keyword(s):  
Heat Shock ◽  
Small Interfering Rna ◽  
Transcriptional Regulators ◽  
Cell Cycle Regulators ◽  
Anaphase Promoting Complex ◽  
Acute Response ◽  
Ubiquitin E3 Ligase ◽  
Shock Response ◽  
C Subunit ◽  
Interfering Rna

ABSTRACT The ubiquitin E3 ligase anaphase-promoting complex/cyclosome (APC/C) drives degradation of cell cycle regulators in cycling cells by associating with the coactivators Cdc20 and Cdh1. Although a plethora of APC/C substrates have been identified, only a few transcriptional regulators are described as direct targets of APC/C-dependent ubiquitination. Here we show that APC/C, through substrate recognition by both Cdc20 and Cdh1, mediates ubiquitination and degradation of heat shock factor 2 (HSF2), a transcription factor that binds to the Hsp70 promoter. The interaction between HSF2 and the APC/C subunit Cdc27 and coactivator Cdc20 is enhanced by moderate heat stress, and the degradation of HSF2 is induced during the acute phase of the heat shock response, leading to clearance of HSF2 from the Hsp70 promoter. Remarkably, Cdc20 and the proteasome 20S core α2 subunit are recruited to the Hsp70 promoter in a heat shock-inducible manner. Moreover, the heat shock-induced expression of Hsp70 is increased when Cdc20 is silenced by a specific small interfering RNA (siRNA). Our results provide the first evidence for participation of APC/C in the acute response to protein-damaging stress.

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